Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein HEG homolog 1

Gene

HEG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity May act through the stabilization of endothelial cell junctions.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Protein HEG homolog 1
Gene namesi
Name:HEG1
Synonyms:KIAA1237
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:29227. HEG1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 12481219ExtracellularSequence analysisAdd
BLAST
Transmembranei1249 – 126921HelicalSequence analysisAdd
BLAST
Topological domaini1270 – 1381112CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671699.

Polymorphism and mutation databases

BioMutaiHEG1.
DMDMi147645934.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 13811352Protein HEG homolog 1PRO_0000286981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi67 – 671O-linked (GalNAc...)1 Publication
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence analysis
Glycosylationi159 – 1591N-linked (GlcNAc...)1 Publication
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence analysis
Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)1 Publication
Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi989 ↔ 1000PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1011PROSITE-ProRule annotation
Disulfide bondi1013 ↔ 1022PROSITE-ProRule annotation
Disulfide bondi1029 ↔ 1040PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1049PROSITE-ProRule annotation
Disulfide bondi1051 ↔ 1062PROSITE-ProRule annotation
Glycosylationi1137 – 11371N-linked (GlcNAc...)Sequence analysis
Modified residuei1359 – 13591PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9ULI3.
MaxQBiQ9ULI3.
PaxDbiQ9ULI3.
PRIDEiQ9ULI3.

PTM databases

iPTMnetiQ9ULI3.
PhosphoSiteiQ9ULI3.
SwissPalmiQ9ULI3.
UniCarbKBiQ9ULI3.

Expressioni

Gene expression databases

BgeeiQ9ULI3.
CleanExiHS_HEG1.
ExpressionAtlasiQ9ULI3. baseline and differential.
GenevisibleiQ9ULI3. HS.

Organism-specific databases

HPAiHPA011559.

Interactioni

Subunit structurei

Interacts with CCM2 and KRIT1; KRIT1 markedly facilitates interaction with CCM2.1 Publication

Protein-protein interaction databases

BioGridi121560. 3 interactions.
STRINGi9606.ENSP00000311502.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U7DX-ray2.49B/D1356-1381[»]
4HDQX-ray1.95C1356-1381[»]
ProteinModelPortaliQ9ULI3.
SMRiQ9ULI3. Positions 986-1056, 1182-1219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini985 – 102339EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1025 – 106339EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi463 – 743281Ser-richAdd
BLAST

Sequence similaritiesi

Contains 2 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJZT. Eukaryota.
ENOG410Y1MK. LUCA.
GeneTreeiENSGT00710000106813.
HOGENOMiHOG000112879.
InParanoidiQ9ULI3.
OMAiFWQNDSP.
OrthoDBiEOG7N8ZV7.
PhylomeDBiQ9ULI3.
TreeFamiTF335941.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR028720. HEG.
[Graphical view]
PANTHERiPTHR24037. PTHR24037. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULI3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPRASRWP PPLLLLLLPL LLLPPAAPGT RDPPPSPARR ALSLAPLAGA
60 70 80 90 100
GLELQLERRP EREPPPTPPR ERRGPATPGP SYRAPEPGAA TQRGPSGRAP
110 120 130 140 150
RGGSADAAWK HWPESNTEAH VENITFYQNQ EDFSTVSSKE GVMVQTSGKS
160 170 180 190 200
HAASDAPENL TLLAETADAR GRSGSSSRTN FTILPVGYSL EIATALTSQS
210 220 230 240 250
GNLASESLHL PSSSSEFDER IAAFQTKSGT ASEMGTERAM GLSEEWTVHS
260 270 280 290 300
QEATTSAWSP SFLPALEMGE LTTPSRKRNS SGPDLSWLHF YRTAASSPLL
310 320 330 340 350
DLSSSSESTE KLNNSTGLQS SSVSQTKTMH VATVFTDGGP RTLRSLTVSL
360 370 380 390 400
GPVSKTEGFP KDSRIATTSS SVLLSPSAVE SRRNSRVTGN PGDEEFIEPS
410 420 430 440 450
TENEFGLTSL RWQNDSPTFG EHQLASSSEV QNGSPMSQTE TVSRSVAPMR
460 470 480 490 500
GGEITAHWLL TNSTTSADVT GSSASYPEGV NASVLTQFSD STVQSGGSHT
510 520 530 540 550
ALGDRSYSES SSTSSSESLN SSAPRGERSI AGISYGQVRG TAIEQRTSSD
560 570 580 590 600
HTDHTYLSST FTKGERALLS ITDNSSSSDI VESSTSYIKI SNSSHSEYSS
610 620 630 640 650
FFHAQTERSN ISSYDGEYAQ PSTESPVLHT SNLPSYTPTI NMPNTSVVLD
660 670 680 690 700
TDAEFVSDSS SSSSSSSSSS SSGPPLPLPS VSQSHHLFSS ILPSTRASVH
710 720 730 740 750
LLKSTSDAST PWSSSPSPLP VSLTTSTSAP LSVSQTTLPQ SSSTPVLPRA
760 770 780 790 800
RETPVTSFQT STMTSFMTML HSSQTADLKS QSTPHQEKVI TESKSPSLVS
810 820 830 840 850
LPTESTKAVT TNSPLPPSLT ESSTEQTLPA TSTNLAQMSP TFTTTILKTS
860 870 880 890 900
QPLMTTPGTL SSTASLVTGP IAVQTTAGKQ LSLTHPEILV PQISTEGGIS
910 920 930 940 950
TERNRVIVDA TTGLIPLTSV PTSAKEMTTK LGVTAEYSPA SRSLGTSPSP
960 970 980 990 1000
QTTVVSTAED LAPKSATFAV QSSTQSPTTV SSSASVNSCA VNPCLHNGEC
1010 1020 1030 1040 1050
VADNTSRGYH CRCPPSWQGD DCSVDVNECL SNPCPSTAMC NNTQGSFICK
1060 1070 1080 1090 1100
CPVGYQLEKG ICNLVRTFVT EFKLKRTFLN TTVEKHSDLQ EVENEITKTL
1110 1120 1130 1140 1150
NMCFSALPSY IRSTVHASRE SNAVVISLQT TFSLASNVTL FDLADRMQKC
1160 1170 1180 1190 1200
VNSCKSSAEV CQLLGSQRRI FRAGSLCKRK SPECDKDTSI CTDLDGVALC
1210 1220 1230 1240 1250
QCKSGYFQFN KMDHSCRACE DGYRLENETC MSCPFGLGGL NCGNPYQLIT
1260 1270 1280 1290 1300
VVIAAAGGGL LLILGIALIV TCCRKNKNDI SKLIFKSGDF QMSPYAEYPK
1310 1320 1330 1340 1350
NPRSQEWGRE AIEMHENGST KNLLQMTDVY YSPTSVRNPE LERNGLYPAY
1360 1370 1380
TGLPGSRHSC IFPGQYNPSF ISDESRRRDY F
Length:1,381
Mass (Da):147,461
Last modified:May 15, 2007 - v3
Checksum:i2E8402AC5227F95C
GO
Isoform 2 (identifier: Q9ULI3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     986-1012: VNSCAVNPCLHNGECVADNTSRGYHCR → GKTQSHKHMLTARPSPALRATWGSGFM
     1013-1381: Missing.

Note: No experimental confirmation available.
Show »
Length:1,012
Mass (Da):106,446
Checksum:i624A3558CCCACE33
GO

Sequence cautioni

The sequence AAH67235.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11336.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451Q → R.
Corresponds to variant rs4404487 [ dbSNP | Ensembl ].
VAR_048984
Natural varianti305 – 3051S → P.
Corresponds to variant rs2981546 [ dbSNP | Ensembl ].
VAR_059269
Natural varianti602 – 6021F → S.
Corresponds to variant rs6790837 [ dbSNP | Ensembl ].
VAR_032253
Natural varianti980 – 9801V → L.1 Publication
Corresponds to variant rs10804567 [ dbSNP | Ensembl ].
VAR_032254
Natural varianti1039 – 10391M → T.
Corresponds to variant rs6438869 [ dbSNP | Ensembl ].
VAR_032255

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei986 – 101227VNSCA…GYHCR → GKTQSHKHMLTARPSPALRA TWGSGFM in isoform 2. 1 PublicationVSP_025275Add
BLAST
Alternative sequencei1013 – 1381369Missing in isoform 2. 1 PublicationVSP_025276Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC026342 Genomic DNA. No translation available.
AC092983 Genomic DNA. No translation available.
AC117488 Genomic DNA. No translation available.
AB033063 mRNA. Translation: BAA86551.2.
AK074987 mRNA. Translation: BAC11336.1. Different initiation.
BC004539 mRNA. Translation: AAH04539.2.
BC067235 mRNA. Translation: AAH67235.1. Different initiation.
CCDSiCCDS46898.1. [Q9ULI3-1]
RefSeqiNP_065784.1. NM_020733.1. [Q9ULI3-1]
UniGeneiHs.477420.

Genome annotation databases

EnsembliENST00000311127; ENSP00000311502; ENSG00000173706. [Q9ULI3-1]
GeneIDi57493.
KEGGihsa:57493.
UCSCiuc003ehs.4. human. [Q9ULI3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC026342 Genomic DNA. No translation available.
AC092983 Genomic DNA. No translation available.
AC117488 Genomic DNA. No translation available.
AB033063 mRNA. Translation: BAA86551.2.
AK074987 mRNA. Translation: BAC11336.1. Different initiation.
BC004539 mRNA. Translation: AAH04539.2.
BC067235 mRNA. Translation: AAH67235.1. Different initiation.
CCDSiCCDS46898.1. [Q9ULI3-1]
RefSeqiNP_065784.1. NM_020733.1. [Q9ULI3-1]
UniGeneiHs.477420.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U7DX-ray2.49B/D1356-1381[»]
4HDQX-ray1.95C1356-1381[»]
ProteinModelPortaliQ9ULI3.
SMRiQ9ULI3. Positions 986-1056, 1182-1219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121560. 3 interactions.
STRINGi9606.ENSP00000311502.

PTM databases

iPTMnetiQ9ULI3.
PhosphoSiteiQ9ULI3.
SwissPalmiQ9ULI3.
UniCarbKBiQ9ULI3.

Polymorphism and mutation databases

BioMutaiHEG1.
DMDMi147645934.

Proteomic databases

EPDiQ9ULI3.
MaxQBiQ9ULI3.
PaxDbiQ9ULI3.
PRIDEiQ9ULI3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311127; ENSP00000311502; ENSG00000173706. [Q9ULI3-1]
GeneIDi57493.
KEGGihsa:57493.
UCSCiuc003ehs.4. human. [Q9ULI3-1]

Organism-specific databases

CTDi57493.
GeneCardsiHEG1.
H-InvDBHIX0003945.
HGNCiHGNC:29227. HEG1.
HPAiHPA011559.
MIMi614182. gene.
neXtProtiNX_Q9ULI3.
PharmGKBiPA142671699.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJZT. Eukaryota.
ENOG410Y1MK. LUCA.
GeneTreeiENSGT00710000106813.
HOGENOMiHOG000112879.
InParanoidiQ9ULI3.
OMAiFWQNDSP.
OrthoDBiEOG7N8ZV7.
PhylomeDBiQ9ULI3.
TreeFamiTF335941.

Miscellaneous databases

ChiTaRSiHEG1. human.
GenomeRNAii57493.
PROiQ9ULI3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULI3.
CleanExiHS_HEG1.
ExpressionAtlasiQ9ULI3. baseline and differential.
GenevisibleiQ9ULI3. HS.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR028720. HEG.
[Graphical view]
PANTHERiPTHR24037. PTHR24037. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-1381.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1117-1381.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1381 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1140-1381 (ISOFORM 1), VARIANT LEU-980.
    Tissue: Kidney and Ovary.
  5. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-159 AND ASN-520.
    Tissue: Plasma.
  6. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-67, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Structural basis of the junctional anchorage of the cerebral cavernous malformations complex."
    Gingras A.R., Liu J.J., Ginsberg M.H.
    J. Cell Biol. 199:39-48(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1356-1381 IN COMPLEX WITH KRIT1, INTERACTION WITH KRIT1.

Entry informationi

Entry nameiHEG1_HUMAN
AccessioniPrimary (citable) accession number: Q9ULI3
Secondary accession number(s): Q6NX66, Q8NC40, Q9BSV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.